Modeling based on the structure of vicilins predicts a histidine cluster in the active site of oxalate oxidase
Modeling based on the structure of vicilins predicts a histidine cluster in the active site of oxalate oxidase
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DOI：
10.1007/pl00006329
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发表时间：
1998-04-01
影响因子：
3.9
通讯作者：
Warwicker, J
中科院分区：
文献类型：
--
作者：
Gane, PJ;Dunwell, JM;Warwicker, J
已知芽蛋白是一种草酸氧化酶，它是发芽小麦中生长开始的标志物，并且芽蛋白与豆球蛋白和豌豆球蛋白种子储存蛋白具有序列相似性。将这两条信息组合起来，以便生成基于豌豆球蛋白结构的胚蛋白 3D 模型，并检查该模型的潜在草酸氧化酶活性位点。三个组氨酸残基的簇位于保守的β-桶结构内。虽然模型和豌豆球蛋白结构之间总体序列相似性水平相对较低，但对于维持 β-桶支架重要的氨基酸的保守性为组氨酸残基的并置提供了信心。该簇在结构上与铜胺氧化酶和其他蛋白质中发现的簇相似，因此表明它在草酸氧化酶活性位点内定义了金属结合位置。还提出参与豌豆球蛋白分子间相互作用的结构元件可能在胚芽蛋白/草酸氧化酶的寡聚体形成中发挥作用。
It is known that germin, which is a marker of the onset of growth in germinating wheat, is an oxalate oxidase, and also that germins possess sequence similarity with legumin and vicilin seed storage proteins. These two pieces of Information have been combined in order to generate a 3D model of germin based on the structure of vicilin and to examine the model with regard to a potential oxalate oxidase active site. A cluster of three histidine residues has been located within the conserved beta-barrel structure. While there is a relatively low level of overall sequence similarity between the model and the vicilin structures, the conservation of amino acids important in maintaining the scaffold of the beta-barrel lends confidence to the juxtaposition of the histidine residues. The cluster is similar structurally to those found in copper amine oxidase and other proteins, leading to the suggestion that it defines a metal-binding location within the oxalate oxidase active site. It is also proposed that the structural elements involved in Intermolecular interactions in vicilins may play a role in oligomer formation in germin/oxalate oxidase.